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Conserved domains on  [gi|1370515101|ref|XP_024303445|]
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histone-lysine N-methyltransferase EHMT1 isoform X18 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
744-974 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


:

Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 823
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 903
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  904 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 974
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
222-352 3.10e-67

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


:

Pssm-ID: 411018  Cd Length: 133  Bit Score: 221.11  E-value: 3.10e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  222 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 300
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  301 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 352
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-684 1.78e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 1.78e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  428 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 507
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  508 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 587
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  588 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 667
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1370515101  668 SRDSDVTLKNKEGETPL 684
Cdd:COG0666    273 LALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
744-974 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 823
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 903
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  904 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 974
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
222-352 3.10e-67

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 221.11  E-value: 3.10e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  222 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 300
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  301 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 352
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-684 1.78e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 1.78e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  428 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 507
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  508 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 587
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  588 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 667
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1370515101  668 SRDSDVTLKNKEGETPL 684
Cdd:COG0666    273 LALLLLAAALLDLLTLL 289
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
834-956 7.06e-40

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 143.63  E-value: 7.06e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101   834 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 905
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1370515101   906 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 956
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
722-826 1.58e-29

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 112.90  E-value: 1.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  722 IARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKDGRL 798
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 1370515101  799 LPEfnmaEPPLIFECNHACSCWRNCRNR 826
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-611 4.31e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 4.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  518 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 597
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1370515101  598 KLLLSKGSDINIRD 611
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
844-973 9.45e-29

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 111.98  E-value: 9.45e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  844 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 918
Cdd:COG2940     16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  919 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 973
Cdd:COG2940     92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
458-691 6.74e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 6.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  458 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 532
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 608
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  609 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 688
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                   ...
gi 1370515101  689 LNS 691
Cdd:PHA03100   234 LNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
516-687 2.19e-13

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 74.28  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  516 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 589
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  590 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 655
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1370515101  656 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 687
Cdd:cd22192    178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
515-610 1.00e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  515 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 581
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 1370515101  582 WTPMIWATEYKHVDLVKLLLSKGSDINIR 610
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
546-576 1.09e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.09e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1370515101   546 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 576
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
 
Name Accession Description Interval E-value
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
744-974 0e+00

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 535.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 823
Cdd:cd10535      1 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 903
Cdd:cd10535     81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  904 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 974
Cdd:cd10535    161 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 231
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
744-974 1.59e-168

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins; This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380941 [Multi-domain]  Cd Length: 231  Bit Score: 491.85  E-value: 1.59e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 823
Cdd:cd10543      1 PDFLYVTENCETSPLNIDRNITSLQTCSCRDDCSSDNCVCGRLSVRCWYDKEGRLLPDFNKLDPPLIFECNRACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 903
Cdd:cd10543     81 RNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSREDDSYLFDLDNKDGETYCIDARRYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  904 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHS 974
Cdd:cd10543    161 SRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYGEKFWRIKGKYFTCRCGSPKCKYS 231
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
744-982 1.31e-155

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins; EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380931 [Multi-domain]  Cd Length: 239  Bit Score: 459.10  E-value: 1.31e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNC 823
Cdd:cd10533      1 EDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNV 903
Cdd:cd10533     81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  904 SRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQ 982
Cdd:cd10533    161 SRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQ 239
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
744-951 9.62e-105

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 325.48  E-value: 9.62e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLS-MRCWYDKDGRLLPefnMAEPPLIFECNHACSCWRN 822
Cdd:cd10538      1 PSFTYIKDNIVGKNVQPFSNIIDSVGCKCKDDCLDSKCACAAESdGIFAYTKNGLLRL---NNSPPPIFECNSKCSCDDD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  823 CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDN-----KDGE 891
Cdd:cd10538     78 CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKiydksgGSYLFDLDEfsdsdGDGE 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  892 VYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 951
Cdd:cd10538    158 ELCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
721-972 5.06e-72

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes.


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 240.27  E-value: 5.06e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  721 DIARGYERIPIPCVNAVDSEPcPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCS-SSNCMCGQLS---MRCWYDKDG 796
Cdd:cd10517      8 DISYGKEGVPIPCVNEIDNSS-PPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRdKSKCACQQLTieaTAATPGGQI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  797 --------RLLPEFnmaEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELI 868
Cdd:cd10517     87 npsagyqyRRLMEK---LPTGVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQIL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  869 SDSEADVREE---DSYLFDLD------------NKDGEVYC--IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPR 931
Cdd:cd10517    164 TEDEANEEGLqygDEYFAELDyievveklkegyESDVEEHCyiIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPW 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1370515101  932 IAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 972
Cdd:cd10517    244 VAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
222-352 3.10e-67

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 221.11  E-value: 3.10e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  222 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 300
Cdd:cd20905      1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  301 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 352
Cdd:cd20905     81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
744-972 3.29e-67

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 225.25  E-value: 3.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNIthLQYCVCIDDC--SSSNCmCGQLS-MRCWYDKDGRLLpeFNMAEPplIFECNHACSCW 820
Cdd:cd10542      1 PNFQYINDYIPGDGVKIPEDF--LVGCECTEDChnNNPTC-CPAESgVKFAYDKQGRLR--LPPGTP--IYECNSRCKCG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  821 RNCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLD-NKDGEV 892
Cdd:cd10542     74 PDCPNRVVQRGRKVPLCIFRTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRgkiydaNGRTYLFDLDyNDDDCE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  893 YCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------GERFWDIKGKLFS 963
Cdd:cd10542    154 YTVDAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYlmtgtggssESTIPKPKDVRVP 233

                   ....*....
gi 1370515101  964 CRCGSPKCR 972
Cdd:cd10542    234 CLCGSKNCR 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-684 1.78e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 1.78e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  428 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 507
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  508 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 587
Cdd:COG0666    114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  588 ATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 667
Cdd:COG0666    193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                          250
                   ....*....|....*..
gi 1370515101  668 SRDSDVTLKNKEGETPL 684
Cdd:COG0666    273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
431-710 2.66e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 2.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  431 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTC 510
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  511 SEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATE 590
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  591 YKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 670
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1370515101  671 SDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDR 710
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
744-972 2.63e-53

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 186.74  E-value: 2.63e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHLQYCVCIDD-CSSSNCMCgqlsMRCW---YDKDGRLLPEF-NMAEPplIFECNHACS 818
Cdd:cd10544      1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSsCEPETCSC----LRKYgpnYDDDGCLLDFDgKYSGP--VFECNSMCK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  819 CWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDN--KDG 890
Cdd:cd10544     75 CSESCQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRtksqtkGDMNYIIVLREhlSSG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  891 EVY--CIDARFYGNVSRFINHHCEPNL--VPVRVfmahqDLRFPRIAFFSTRLIEAGEQLGFDYGERF-----------W 955
Cdd:cd10544    155 KVLetFVDPTYIGNIGRFLNHSCEPNLfmVPVRV-----DSMVPKLALFAARDIVAGEELSFDYSGEFsnsvesvtlarQ 229
                          250
                   ....*....|....*..
gi 1370515101  956 DIKGKLFSCRCGSPKCR 972
Cdd:cd10544    230 DESKSRKPCLCGAENCR 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
463-690 1.56e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 183.23  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  463 LLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDP 542
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  543 KDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAA 622
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  623 FSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 690
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEN 229
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
770-951 1.61e-51

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins; Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380943 [Multi-domain]  Cd Length: 232  Bit Score: 181.06  E-value: 1.61e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  770 CVCIDDC--SSSNCMCGQL-SMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGW 846
Cdd:cd10545     24 CDCKNRCtdGASDCACVKKnGGEIPYNFNGRLI-----RAKPAIYECGPLCKCPPSCYNRVTQKGLRYRLEVFKTAERGW 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  847 GVRSLQDIPPGTFVCEYVGELISDSEADVR-EEDSYLFDLDNK------DGEV---------------------YCIDAR 898
Cdd:cd10545     99 GVRSWDSIPAGSFICEYVGELLDTSEADTRsGNDDYLFDIDNRqtnrgwDGGQrldvgmsdgerssaedeesseFTIDAG 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  899 FYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 951
Cdd:cd10545    179 SFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
770-972 3.29e-49

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 174.27  E-value: 3.29e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  770 CVCIDDC-SSSNCMCGQLSMRCWYDKDG-----------RLLPEfnmAEPPLIFECNHACSCWRN-CRNRVVQNGLRARL 836
Cdd:cd10541     18 CDCTDGCrDKSKCACHQLTIQATACTPGgqdnptagyqyKRLEE---CLPTGVYECNKLCKCDPNmCQNRLVQHGLQVRL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  837 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEAD---VREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEP 913
Cdd:cd10541     95 QLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkegLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSP 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  914 NLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 972
Cdd:cd10541    175 NLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECR 233
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
745-972 2.81e-46

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins; SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 166.61  E-value: 2.81e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  745 NYKYVSQNCVTSPMNIDRNITHlqyCVCiDDCSSS---NCMCGQLSMRCWYDKDGRLLPefnMAEPPlIFECNHACSCWR 821
Cdd:cd10525      2 DFVYINEYKVGEGVTLNQVAVG---CEC-QDCLSQpvgGCCPGASKHRFAYNEQGQVKV---RPGLP-IYECNSRCRCGP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  822 NCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYLFDLDNKDgEVYC 894
Cdd:cd10525     74 DCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVYT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  895 IDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY---------------------GER 953
Cdd:cd10525    153 VDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYnmqvdpvdaestkmdsnfglaGLP 232
                          250
                   ....*....|....*....
gi 1370515101  954 FWDIKGKLFSCRCGSPKCR 972
Cdd:cd10525    233 GSPKKRVRIECKCGVRSCR 251
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
744-972 9.24e-46

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins; SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 164.68  E-value: 9.24e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  744 SNYKYVSQNCVTSPMNIDRNITHlqYCVCIDdCSSSNCMCGQLSMRCWYDKDGRLlpefnMAEPPL-IFECNHACSCWRN 822
Cdd:cd10532      1 IDFYYINEYKPAPGINLDNEATV--GCDCSD-CFFGKCCPAEAGVLFAYNEHGQL-----KIPPGTpIYECNSRCKCGPD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  823 CRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS----YLFDLDNKDGEvYCI 895
Cdd:cd10532     73 CPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQfyDSkgitYLFDLDYESDE-FTV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  896 DARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY-----GERFWDI-------KGKLFS 963
Cdd:cd10532    152 DAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYqmkgsGDLSSDSidnspakKRVRTV 231

                   ....*....
gi 1370515101  964 CRCGSPKCR 972
Cdd:cd10532    232 CKCGAVTCR 240
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
770-972 7.46e-45

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3.


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 163.26  E-value: 7.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  770 CVCIDDCSSSNCMCGQLSMRCWY---DKDGRLLPEFNMAEPPlIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRD-MG 845
Cdd:cd19473     39 CLCLQDVDPDDDRDPGKKKNAYHssgAKKGCLRGHMLNSRLP-IYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDgRG 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  846 WGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLD----------NKDGEVYCIDARFYGNVSRFI 907
Cdd:cd19473    118 WGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaqrkdvYLFALDkfsdpdsldpRLRGDPYEIDGEFMSGPTRFI 197
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  908 NHHCEPNLvpvRVFM---AHQDLRFPRIAFFSTRLIEAGEQLGFDY--------GERFWDIKGK-LFSCRCGSPKCR 972
Cdd:cd19473    198 NHSCDPNL---RIFArvgDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKeMTKCLCGSPKCR 271
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
770-972 1.54e-44

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins; This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog.


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 161.97  E-value: 1.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  770 CVCIDDCSSSNCMcgqlsmrcwYDKDGRLlpefNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVR 849
Cdd:cd20073     42 CQCLEDSNEKSFA---------YDEYGRV----RANTGSIIYECNENCDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLR 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  850 SLQDIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKDGEV---YCIDARFYGNVSRFINHHCEPNLVPVRV 920
Cdd:cd20073    109 CPRFIKAGTFIGVYLGEVITQSEAEIRGKKydnvgvTYLFDLDLFEDQVdeyYTVDAQYCGDVTRFINHSCDPNLAIYSV 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  921 FMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGER----------------FWDIKGKLfSCRCGSPKCR 972
Cdd:cd20073    189 LRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRnnfdqlgfignrsnskYINLKNKR-PCYCGSANCR 255
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
735-972 3.58e-43

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins; SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 158.07  E-value: 3.58e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  735 NAVDSEPCPSNYKYVSQNCVTSpmnidrNITHLQYCVCIDDCSS-SNCMCGQLSMR-------------CWYdKDGRLLp 800
Cdd:cd10523      5 TYVQLDRNPQDQQQLVDDFDIS------NGAFVDSCDCTDGCIDiLKCACLQLTARafsksesspskggRGY-KYKRLQ- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  801 efnMAEPPLIFECNHACSCWRN-CRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELIS---------- 869
Cdd:cd10523     77 ---EPIPSGLYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSrarspteplp 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  870 -------DSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEA 942
Cdd:cd10523    154 pklelpsENEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKA 233
                          250       260       270
                   ....*....|....*....|....*....|
gi 1370515101  943 GEQLGFDYGERFWDIKGKLFSCRCGSPKCR 972
Cdd:cd10523    234 GTELTWDYSYDAGTSPEQEIPCLCGVNKCQ 263
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
834-956 7.06e-40

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 143.63  E-value: 7.06e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101   834 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCIDARFYGNVSR 905
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKaydtdgakAFYLFDIDSD----LCIDARRKGNLAR 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1370515101   906 FINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 956
Cdd:smart00317   77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYGSDYAN 123
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
836-972 1.73e-36

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 134.30  E-value: 1.73e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  836 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLdnKDGEVycIDARFYGNVSRFI 907
Cdd:cd10531      2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERldeyeelgKSNFYILSL--SDDVV--IDATRKGNLSRFI 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  908 NHHCEPNLVpVRVFMAhqdLRFPRIAFFSTRLIEAGEQLGFDYGerFWDIKGKLFSCRCGSPKCR 972
Cdd:cd10531     78 NHSCEPNCE-TQKWIV---NGEYRIGIFALRDIPAGEELTFDYN--FVNYNEAKQVCLCGAQNCR 136
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
824-972 7.85e-34

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 127.33  E-value: 7.85e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKdgevYCI 895
Cdd:cd10518      4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKrydeegggGTYMFRIDED----LVI 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  896 DARFYGNVSRFINHHCEPNLVpVRVfMAHQDLRfpRIAFFSTRLIEAGEQLGFDYgeRFWDIKGKLFSCRCGSPKCR 972
Cdd:cd10518     80 DATKKGNIARFINHSCDPNCY-AKI-ITVDGEK--HIVIFAKRDIAPGEELTYDY--KFPIEDEEKIPCLCGAPNCR 150
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
836-972 3.96e-33

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 124.71  E-value: 3.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  836 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNkdgevYC--------IDARFYGNVSRFI 907
Cdd:cd19174      2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH-----YClnldsgmvIDGYRMGNEARFV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  908 NHHCEPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19174     77 NHSCDPNCEMQKWSVNGV----YRIGLFALKDIPAGEELTYDYNFHSFNVEKQQ-PCKCGSPNCR 136
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
834-972 4.44e-31

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 118.84  E-value: 4.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  834 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKDgevyCIDARFYGNVSR 905
Cdd:cd19172      2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYaregnrhyYFMALKSDE----IIDATKKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  906 FINHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYG-ERFWDIKGKlfsCRCGSPKCR 972
Cdd:cd19172     78 FINHSCEPNCE-TQKWTVNGEL---RVGFFAKRDIPAGEELTFDYQfERYGKEAQK---CYCGSPNCR 138
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
722-826 1.58e-29

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 112.90  E-value: 1.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  722 IARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRnithLQYCVCiDDCSSSNCMCGQLSM---RCWYDKDGRL 798
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII----PQGCDC-GDCSSEKCSCAQLNGgefRFPYDKDGLL 75
                           90       100
                   ....*....|....*....|....*...
gi 1370515101  799 LPEfnmaEPPLIFECNHACSCWRNCRNR 826
Cdd:pfam05033   76 VPE----SKPPIYECNPLCGCPPSCPNR 99
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
845-951 2.81e-29

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 113.00  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVCEYVGE-LISDSEADVREE-----------DSYLFDLDNKDGevYCIDAR--FYGNVSRFINHH 910
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELlyydklelrlwGPYLFTLDEDSE--YCIDARalYYGNWARFINHS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370515101  911 CEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYG 951
Cdd:pfam00856   79 CDPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-611 4.31e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 4.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  518 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 597
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1370515101  598 KLLLSKGSDINIRD 611
Cdd:pfam12796   78 KLLLEKGADINVKD 91
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
844-973 9.45e-29

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 111.98  E-value: 9.45e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  844 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-----YLFDLDnkDGEVycIDARFYGNVSRFINHHCEPNLVPV 918
Cdd:COG2940     16 HGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKeplhtYLFELD--DDGV--IDGALGGNPARFINHSCDPNCEAD 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  919 RvfmahqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDikgKLFSCRCgsPKCRH 973
Cdd:COG2940     92 E--------EDGRIFIVALRDIAAGEELTYDYGLDYDE---EEYPCRC--PNCRG 133
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
835-951 3.79e-27

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 106.94  E-value: 3.79e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  835 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE--ED----SYLFDLDNKdgevYCIDARFYGNVSRFIN 908
Cdd:cd10519      2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGkiYDkynsSYLFNLNDQ----FVVDATRKGNKIRFAN 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370515101  909 HHCEPNLVPvRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYG 951
Cdd:cd10519     78 HSSNPNCYA-KVMMVNGD---HRIGIFAKRDIEAGEELFFDYG 116
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
720-818 3.25e-26

N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal to some SET domains. Function is unknown. Unpublished.


Pssm-ID: 128744 [Multi-domain]  Cd Length: 98  Bit Score: 103.65  E-value: 3.25e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101   720 RDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSN-CMCGQLSMRCW-YDKDGR 797
Cdd:smart00468    2 LDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNkCECARKNGGEFaYELNGG 81
                            90       100
                    ....*....|....*....|.
gi 1370515101   798 LLPEfnmaEPPLIFECNHACS 818
Cdd:smart00468   82 LRLK----RKPLIYECNSRCS 98
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
834-971 5.72e-26

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins; The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B) or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3.


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 104.32  E-value: 5.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  834 ARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS--------YLFDLDNKdgevYCIDARFYGNVSR 905
Cdd:cd19173      2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAhennitnfYMLTLDKD----RIIDAGPKGNLSR 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  906 FINHHCEPNLvPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKG-KLFSCRCGSPKC 971
Cdd:cd19173     78 FMNHSCQPNC-ETQKWTVNGD---TRVGLFAVRDIPAGEELTFNYN---LDCLGnEKKVCRCGAPNC 137
PHA03100 PHA03100
ankyrin repeat protein; Provisional
458-691 6.74e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.68  E-value: 6.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  458 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 532
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 608
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  609 IRDNeeniclhwaafsgcvdiAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCAS 688
Cdd:PHA03100   171 AKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233

                   ...
gi 1370515101  689 LNS 691
Cdd:PHA03100   234 LNN 236
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
835-972 2.01e-25

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 102.88  E-value: 2.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  835 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR--------EEDSYLFDLDnKDgevYCIDARFYGNVSRF 906
Cdd:cd19175      1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERlwdmkhkgEKNFYMCEID-KD---MVIDATFKGNLSRF 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  907 INHHCEPNLVpVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYgeRFWDIkGKLFSCRCGSPKCR 972
Cdd:cd19175     77 INHSCDPNCE-LQKWQVDGET---RIGVFAIRDIKKGEELTYDY--QFVQF-GADQDCHCGSKNCR 135
Ank_2 pfam12796
Ankyrin repeats (3 copies);
485-578 3.29e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.19  E-value: 3.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  485 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKaGALVDPKDaEGSTCLHLAAKKGHYEVVQ 564
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....
gi 1370515101  565 YLLSNGQmDVNCQD 578
Cdd:pfam12796   79 LLLEKGA-DINVKD 91
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
830-972 3.51e-24

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 99.33  E-value: 3.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  830 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 898
Cdd:cd19169      6 NQLKFRkkqLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKryeaigigSSYLFRVD----DDTIIDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  899 FYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 972
Cdd:cd19169     82 KCGNLARFINHSCNPNCYAKIITVESQK----KIVIYSKRPIAVNEEITYDYKFPIEDEK---IPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
833-972 1.20e-23

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 98.27  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  833 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDS----YLFDLDNKdgevYCIDARFYGNVSR 905
Cdd:cd19171     13 RSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREkiyESQnrgiYMFRIDND----WVIDATMTGGPAR 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  906 FINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19171     89 YINHSCNPNCV-AEVVTFDKE---KKIIIISNRRIAKGEELTYDYKFDFEDDQHKI-PCLCGAPNCR 150
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
845-956 5.99e-23

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 95.10  E-value: 5.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVCEYVGELISD--SEADVREEDSYLFDLDNKDGEVYcIDARFYGNVSRFINHHCEPNLVPVRVFM 922
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRweEDRDSVYHYDPLYPFDLNGDILV-IDAGKKGNLTRFINHSDQPNLELIVRTL 92
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1370515101  923 AHQdlrfPRIAFFSTRLIEAGEQLGFDYGERFWD 956
Cdd:cd10522     93 KGE----QHIGFVAIRDIKPGEELFISYGPKYWK 122
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
826-953 1.18e-22

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 94.95  E-value: 1.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  826 RVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE----DS------YLFDLDNKDgevYCI 895
Cdd:cd10528      9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlyakDPstgcymYYFQYKGKT---YCV 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  896 DA-RFYGNVSRFINHHC-EPNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGER 953
Cdd:cd10528     86 DAtKESGRLGRLINHSKkKPNLKTKLLVIDGV----PHLILVAKRDIKPGEELLYDYGDR 141
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
830-972 3.51e-22

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).


Pssm-ID: 380998  Cd Length: 148  Bit Score: 93.64  E-value: 3.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  830 NGLRAR---LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDnkdgEVYCIDAR 898
Cdd:cd20072      6 NQLKKRkkqLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKrylrqgigSSYLFRID----DDTVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  899 FYGNVSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 972
Cdd:cd20072     82 KKGNIARFINHCCDPNCT-AKIIKVEGE---KRIVIYAKRDIAAGEELTYDYKFPREEDK---IPCLCGAPNCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
824-972 9.58e-22

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 92.45  E-value: 9.58e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkdgEVYCID 896
Cdd:cd19170      4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKyyESkgigcYMFRID----DDEVVD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  897 ARFYGNVSRFINHHCEPNLVPvRVFmaHQDLRfPRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 972
Cdd:cd19170     80 ATMHGNAARFINHSCEPNCYS-RVV--NIDGK-KHIVIFALRRILRGEELTYDYKFPIEDVK---IPCTCGSKKCR 148
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
845-954 2.47e-21

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 90.33  E-value: 2.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVCEYVGELISDSEADVRE------EDSYLFDLDNKdgevYCIDARFYGNVSRFINHHCEP----N 914
Cdd:cd19168     13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREhrrgdvSYLYLFEEQEG----IWVDAAIYGNLSRYINHATDKvktgN 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370515101  915 LVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGERF 954
Cdd:cd19168     89 CMPKIMYVNHE----WRIKFTAIKDIKIGEELFFNYGDNF 124
PHA03100 PHA03100
ankyrin repeat protein; Provisional
452-644 1.65e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.50  E-value: 1.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  452 FSARQGELQKVLLMLVD-GIDPNFKMEhqNKRSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 524
Cdd:PHA03100    40 YLAKEARNIDVVKILLDnGADINSSTK--NNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  525 -NHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV------------------VQYLLSNGqMDVNCQDDGGWTPM 585
Cdd:PHA03100   118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  586 IWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVN 644
Cdd:PHA03100   197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
837-971 8.94e-20

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 86.58  E-value: 8.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  837 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS---YLFDLDnKDgevYCIDARFYGNVSRFIN 908
Cdd:cd19211      5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARikhahENDIthfYMLTID-KD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  909 HHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFS-CRCGSPKC 971
Cdd:cd19211     81 HSCQPN-CETQKWTVNGD---TRVGLFAVCDIPAGTELTFNYN---LDCLGNEKTvCRCGAPNC 137
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
824-972 1.43e-19

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 86.61  E-value: 1.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDnkDGEVycID 896
Cdd:cd19206      4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKyyDSkgigcYMFRID--DSEV--VD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  897 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19206     80 ATMHGNAARFINHSCEPNCYSRVINIDGQK----HIVIFAMRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKKCR 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
585-677 5.49e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  585 MIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLaAKCDLHAVNiHGDSPLHIAARENRYDCVV 664
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1370515101  665 LFLSRDSDVTLKN 677
Cdd:pfam12796   79 LLLEKGADINVKD 91
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
836-971 1.77e-18

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 83.05  E-value: 1.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  836 LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EED---SYLFDLDnKDgevYCIDARFYGNVSRFI 907
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDitnFYMLTLD-KD---RIIDAGPKGNYARFM 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  908 NHHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDiKGKLfSCRCGSPKC 971
Cdd:cd19210     80 NHCCQPN-CETQKWTVNGD---TRVGLFALCDIKAGTELTFNYNLECLG-NGKT-VCKCGAPNC 137
PHA02874 PHA02874
ankyrin repeat protein; Provisional
455-714 4.96e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.10  E-value: 4.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  455 RQGELQKVLLMLVDGIDPNfkmeHQNKR--SPLHAAAEAGHVDICHMLVQAGANidtcsedqrTPLMEAAENNHlEAVKY 532
Cdd:PHA02874    44 RSGDAKIVELFIKHGADIN----HINTKipHPLLTAIKIGAHDIIKLLIDNGVD---------TSILPIPCIEK-DMIKT 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 612
Cdd:PHA02874   110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  613 eeniclhwaafsgcvdiaeillaakcdlhavniHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASL-NS 691
Cdd:PHA02874   189 ---------------------------------NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNR 235
                          250       260
                   ....*....|....*....|...
gi 1370515101  692 QVWSALQMSKALQDSAPDRPSPV 714
Cdd:PHA02874   236 SAIELLINNASINDQDIDGSTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
450-544 2.09e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  450 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLEA 529
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 1370515101  530 VKYLIKAGALVDPKD 544
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
829-950 3.57e-17

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380994  Cd Length: 136  Bit Score: 78.96  E-value: 3.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  829 QNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE------DSYLFDLDNKdgevYCIDARFYGN 902
Cdd:cd19217      1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKvydkymSSFLFNLNND----FVVDATRKGN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370515101  903 VSRFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 950
Cdd:cd19217     77 KIRFANHSVNPNCY-AKVVMVNGD---HRIGIFAKRAIQQGEELFFDY 120
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
831-950 3.30e-16

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 75.72  E-value: 3.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  831 GLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED------SYLFDLDNKdgevYCIDARFYGNVS 904
Cdd:cd19218      1 GSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVydkymcSFLFNLNND----FVVDATRKGNKI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1370515101  905 RFINHHCEPNLVpVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDY 950
Cdd:cd19218     77 RFANHSVNPNCY-AKVMMVNGD---HRIGIFAKRAIQTGEELFFDY 118
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
837-971 4.37e-16

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 76.12  E-value: 4.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  837 QLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR----EEDS----YLFDLdNKDgevYCIDARFYGNVSRFIN 908
Cdd:cd19212      5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRikraHENSvtnfYMLTV-TKD---RIIDAGPKGNYSRFMN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  909 HHCEPNlVPVRVFMAHQDLrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGK-LFSCRCGSPKC 971
Cdd:cd19212     81 HSCNPN-CETQKWTVNGDV---RVGLFALCDIPAGMELTFNYN---LDCLGNgRTECHCGADNC 137
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
821-972 5.28e-16

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 76.20  E-value: 5.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  821 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 893
Cdd:cd19208      2 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRIDND----H 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  894 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19208     78 VIDATLTGGPARYINHSCAPNCVAEVVTFEKGH----KIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 151
PHA02874 PHA02874
ankyrin repeat protein; Provisional
465-683 6.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.55  E-value: 6.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  465 MLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKD 544
Cdd:PHA02874   110 ILDCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  545 AEGSTCLHLAAKKGHYEVVQYLLSNG-QMDVNCQDdgGWTPMIWATEYKHvDLVKLLLSKGSdINIRDNEENICLHWAAF 623
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGnHIMNKCKN--GFTPLHNAIIHNR-SAIELLINNAS-INDQDIDGSTPLHHAIN 263
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  624 SGC-VDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSrdSDVTLKNKEGETP 683
Cdd:PHA02874   264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
821-972 7.59e-16

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 75.89  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  821 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 893
Cdd:cd19209      3 KSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  894 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19209     79 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 152
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
847-950 7.69e-16

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 75.00  E-value: 7.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  847 GVRSLQDIPPGTFVCEYVGELISDSEADVREE-----DSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVRVF 921
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGffkrpSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPN-AELRHV 96
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1370515101  922 MAHQDlrFPRIAFFSTRLIEAGEQ--LGFDY 950
Cdd:cd10529     97 VVSNG--ELRLFIFALKDIRKGTEitIPFDY 125
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
833-972 1.08e-15

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 75.45  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  833 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 904
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKryvqegigSSYLFRVDHDT----IIDATKCGNLA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  905 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 972
Cdd:cd19204     89 RFINHCCTPNCYAKVITIESQK----KIVIYSKQPIGVNEEITYDYK---FPIEDNKIPCLCGTENCR 149
PHA03095 PHA03095
ankyrin-like protein; Provisional
519-684 1.35e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  519 MEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHY---EVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHV- 594
Cdd:PHA03095    19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTl 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  595 DLVKLLLSKGSDINIRDNEENICLHWAAFSGCVD--IAEILLAAKCDLHAVNIHGDSPLHIAARENRYD--CVVLFLSRD 670
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAG 177
                          170
                   ....*....|....
gi 1370515101  671 SDVTLKNKEGETPL 684
Cdd:PHA03095   178 ADVYAVDDRFRSLL 191
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
847-958 4.22e-15

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 74.36  E-value: 4.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  847 GVRSLQDIPPGTFVCEYVGELISdseadvreEDSYLFDLDNKDGE-------VY-------CIDARFYGNVSRFINHHCE 912
Cdd:cd19183     15 GLFADRPIPAGDPIQELLGEIGL--------QSEYIADPENQYQIlgapkphVFfhpqsplYIDTRRSGSVARFIRRSCR 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370515101  913 PN--LVPVRVfmahQDLRFPRIAFFSTRLIEAGEQLGFDYGerfWDIK 958
Cdd:cd19183     87 PNaeLVTVAS----DSGSVLKFVLYASRDISPGEEITIGWD---WDNP 127
PHA02876 PHA02876
ankyrin repeat protein; Provisional
455-709 4.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 4.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  455 RQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGA--------------------NIDTCSE-- 512
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGAdvniialddlsvlecavdskNIDTIKAii 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  513 DQRT-------PLMEAAENNHLEA----------------------------------VKYLIKAGALVDPKDAEGSTCL 551
Cdd:PHA02876   232 DNRSninkndlSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlVPKLLERGADVNAKNIKGETPL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  552 HLAAKKGH-YEVVQYLLSNGQmDVNCQDDGGWTPMIWATEY-KHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDI 629
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGA-DVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  630 AEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSqvwSALQMSKALQDSAP 708
Cdd:PHA02876   391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN---CKLDVIEMLLDNGA 467

                   .
gi 1370515101  709 D 709
Cdd:PHA02876   468 D 468
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
824-972 7.88e-15

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 72.75  E-value: 7.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  824 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCID 896
Cdd:cd19207      4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydskgiGCYMFRIDDFD----VVD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  897 ARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 972
Cdd:cd19207     80 ATMHGNAARFINHSCEPNCYSRVIHVEGQK----HIVIFALRKIYRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 150
PHA02874 PHA02874
ankyrin repeat protein; Provisional
415-613 1.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  415 PTPGLSQGPGKETLESAlIALDSEKPKKLRFhpkqLYFSARQGELQKVLLMLVDGIDPNfkMEHQNKRSPLHAAAEAGHV 494
Cdd:PHA02874    98 PIPCIEKDMIKTILDCG-IDVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFF 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  495 DICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHyEVVQYLLSNGQmdV 574
Cdd:PHA02874   171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--I 247
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1370515101  575 NCQDDGGWTPMIWATEYK-HVDLVKLLLSKGSDINIRDNE 613
Cdd:PHA02874   248 NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNK 287
PHA02875 PHA02875
ankyrin repeat protein; Provisional
457-697 3.41e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 3.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  457 GELQKVLLMLVDGIDPNFKMehQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKA 536
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  537 GALVDP---KDaeGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 613
Cdd:PHA02875    91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  614 ENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGD-SPLHIAARENRYDCVVLFLSRDSD---VTLKNKEGETPLQ---- 685
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDmicn 247
                          250
                   ....*....|...
gi 1370515101  686 -CASLNSQVWSAL 697
Cdd:PHA02875   248 mCTNLESEAIDAL 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
480-675 3.96e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 3.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  480 NKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGH 559
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  560 YEVVQYLLSNGQM--DVNCQDdgGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 637
Cdd:PHA02875    81 VKAVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370515101  638 CDLHAVNIHGDSPLHIA-ARENRYDCVVL--------FLSRDSDVTL 675
Cdd:PHA02875   159 ACLDIEDCCGCTPLIIAmAKGDIAICKMLldsganidYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
473-612 7.15e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 7.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  473 NFKMEHQNKRSPLHAAAEA--GHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLE------------------AVKY 532
Cdd:PHA03100    98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNY 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 612
Cdd:PHA03100   178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-669 7.60e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 7.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  461 KVLLMLVD-GIDPNFKmeHQNKRSPLHA--AAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH--LEAVKYLIK 535
Cdd:PHA03095    98 DVIKLLIKaGADVNAK--DKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLID 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  536 AGALVDPKDAEGSTCLHLAAK--KGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEY---KHVDLVKLLLsKGSDINIR 610
Cdd:PHA03095   176 AGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLLI-AGISINAR 253
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  611 DNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSR 669
Cdd:PHA03095   254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
835-951 7.63e-14

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 67.28  E-value: 7.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  835 RLQLYRTRDMGWGVRSLQDIPPGTFVCeyvgelisdseadvreedsylfdldnkdgevycidarfygnVSRFINHHCEPN 914
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPKGEVIG-----------------------------------------LARFINHSCEPN 39
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370515101  915 LVPVRVFmahqDLRFPRIAFFSTRLIEAGEQLGFDYG 951
Cdd:cd08161     40 CEFEEVY----VGGKPRVFIVALRDIKAGEELTVDYG 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
447-688 7.87e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 7.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  447 PKQLYFSARQGELQKVLLMLVD-GIDPNFKmeHQNKRSPLHAAAEAGHV-DICHMLVQAGANIDTCSEDQRTPLME--AA 522
Cdd:PHA03095    50 PLHLYLHYSSEKVKDIVRLLLEaGADVNAP--ERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSG 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  523 ENNHLEAVKYLIKAGALVDPKDAEGSTCLHLaakkghyevvqyLLSNGqmDVNcqddggwtpmiwateykhVDLVKLLLS 602
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV------------LLKSR--NAN------------------VELLRLLID 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  603 KGSDINIRDNEENICLHWAAFSgCVDIAEI---LLAAKCDLHAVNIHGDSPLHIAARENRYDCVVL--FLSRDSDVTLKN 677
Cdd:PHA03095   176 AGADVYAVDDRFRSLLHHHLQS-FKPRARIvreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN 254
                          250
                   ....*....|.
gi 1370515101  678 KEGETPLQCAS 688
Cdd:PHA03095   255 RYGQTPLHYAA 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
482-534 8.42e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.53  E-value: 8.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  482 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLI 534
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
449-634 1.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 1.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  449 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 526
Cdd:PHA02875    71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  527 LEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSD 606
Cdd:PHA02875   148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1370515101  607 INIR---DNEE--------NICLHWAAFSGCVDIAEILL 634
Cdd:PHA02875   228 CNIMfmiEGEEctildmicNMCTNLESEAIDALIADIAI 266
PHA02878 PHA02878
ankyrin repeat protein; Provisional
484-806 1.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 1.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  484 PLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIK-------AGALVDPKDA------EGSTC 550
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvFYTLVAIKDAfnnrnvEIFKI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  551 LHLAAKKGHY------------------EVVQYLLSNGQmDVNCQD-DGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 611
Cdd:PHA02878   120 ILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGA-DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  612 NEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA-ARENRYDCVVLFLSRDSDVTLKNK-EGETPLQCASL 689
Cdd:PHA02878   199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  690 NSQVWSALQMSKALQDSAP-DRPSPVERIVSRdiargyeRIPIPCVNAVDSEPCPSNYKYVSqncVTSPMNIDRNIthlq 768
Cdd:PHA02878   279 SERKLKLLLEYGADINSLNsYKLTPLSSAVKQ-------YLCINIGRILISNICLLKRIKPD---IKNSEGFIDNM---- 344
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1370515101  769 ycvcidDCSSSNCMCGQLSMRCWYD----KDGRLLPEFNMAE 806
Cdd:PHA02878   345 ------DCITSNKRLNQIKDKCEDElnrlASIKITNTYSFDD 380
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
516-687 2.19e-13

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 74.28  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  516 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 589
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  590 EYKHVDLVKLLLSKGSDIN--------IRDNEENICL---HWAAFSGCV---DIAEILLAAKCDLHAVNIHGDSPLHIAA 655
Cdd:cd22192     98 VNQNLNLVRELIARGADVVspratgtfFRPGPKNLIYygeHPLSFAACVgneEIVRLLIEHGADIRAQDSLGNTVLHILV 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1370515101  656 RENR-------YDcvvLFLSRDSDV------TLKNKEGETPLQCA 687
Cdd:cd22192    178 LQPNktfacqmYD---LILSYDKEDdlqpldLVPNNQGLTPFKLA 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
514-567 2.88e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.99  E-value: 2.88e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  514 QRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLL 567
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
833-972 3.74e-13

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 68.16  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  833 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--------DSYLFDLDNKDgevyCIDARFYGNVS 904
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKryedegigSSYMFRVDHDT----IIDATKCGNFA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  905 RFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGerfWDIKGKLFSCRCGSPKCR 972
Cdd:cd19205     89 RFINHSCNPNCYAKVITVESQK----KIVIYSKQHINVNEEITYDYK---FPIEDVKIPCLCGSENCR 149
PHA02878 PHA02878
ankyrin repeat protein; Provisional
458-638 3.79e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  458 ELQKVLLMLVDGIDPNFKMEHQNKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAG 537
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  538 ALVDPKDAEGSTCLHLAAKK-GHYEVVQYLLSNGqMDVNCQDD-GGWTPMiwATEYKHVDLVKLLLSKGSDINIRDNEEN 615
Cdd:PHA02878   225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKL 301
                          170       180
                   ....*....|....*....|....
gi 1370515101  616 ICLHWAAFS-GCVDIAEILLAAKC 638
Cdd:PHA02878   302 TPLSSAVKQyLCINIGRILISNIC 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
618-696 3.24e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.24e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  618 LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDsDVTLKNkEGETPLQCASLNSQVWSA 696
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIV 77
Ank_4 pfam13637
Ankyrin repeats (many copies);
547-601 5.09e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 5.09e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  547 GSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLL 601
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
520-690 2.12e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  520 EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKL 599
Cdd:PHA02876   151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  600 LLSKGSDINIRDneenICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVV-LFLSRDSDVTLKNK 678
Cdd:PHA02876   230 IIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNI 305
                          170
                   ....*....|..
gi 1370515101  679 EGETPLQCASLN 690
Cdd:PHA02876   306 KGETPLYLMAKN 317
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
390-694 1.21e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 65.55  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  390 DDKLQGAASHVPEgfDPTGPAGLGRPTPGLSQGPGKETlesaliALDSEKPKKLRFHPKQLYFSARQGELQKV---LLML 466
Cdd:cd22194      3 DSNIRQCPSGNCD--DMDSPQSPQDDTPSNPNSPSAEL------AKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  467 VDGIDPNFKMEHQNKrsplhaAAEAGHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNHLeaVKYLIKAGalVDPKDAE 546
Cdd:cd22194     75 RRKTDVPDFLMHKLT------ASDTGKT--C--LMKALLNINENTKEIVRILLAFAEENGI--LDRFINAE--YTEEAYE 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  547 GSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQ-----------DDG---GWTPMIWATEYKHVDLVKLLLSKGSD-INIRD 611
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGA-DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTdITSQD 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  612 NEENICLHwaafsGCVDIAEillaakcdlhavnihgDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNS 691
Cdd:cd22194    220 SRGNTVLH-----ALVTVAE----------------DSKTQNDFVKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMG 278

                   ...
gi 1370515101  692 QVW 694
Cdd:cd22194    279 KAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
455-706 1.45e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  455 RQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LEAVKY 532
Cdd:PHA02876   249 RNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAAKKGHY-EVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 611
Cdd:PHA02876   327 LIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  612 NEENICLHWAAF-SGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAREN-RYDCVVLFLSRDSDVTLKNKEGETPLQCA-S 688
Cdd:PHA02876   406 QKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAlE 485
                          250
                   ....*....|....*...
gi 1370515101  689 LNSQVWSALQMSKALQDS 706
Cdd:PHA02876   486 YHGIVNILLHYGAELRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
462-643 4.54e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 4.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  462 VLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLmeaaeNNHLEAVK-------Y 532
Cdd:PHA03095   135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLL-----HHHLQSFKprarivrE 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  533 LIKAGALVDPKDAEGSTCLHLAAKKGHYE---VVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 609
Cdd:PHA03095   208 LIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370515101  610 RDNEENICLHWAAFSGCVDIAEILLAAKCDLHAV 643
Cdd:PHA03095   286 VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
Ank_4 pfam13637
Ankyrin repeats (many copies);
617-667 3.43e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  617 CLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFL 667
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
494-614 3.68e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 3.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  494 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LEAVKYLIKAGALVDPKDAEGST---CLHLAAKKGHYEVVQY 565
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370515101  566 LLSNGqMDVNCQDDGGWTPM-IWATEYKHVDL--VKLLLSKGSDINIRDNEE 614
Cdd:PHA02798   131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIDIeiIKLLLEKGVDINTHNNKE 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
477-694 3.94e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  477 EHQNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 554
Cdd:PLN03192   519 EHDDPNmaSNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  555 AKKGHYEVVQYL-----LSNGQM--DVNCQddggwtpmiwATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCV 627
Cdd:PLN03192   599 ISAKHHKIFRILyhfasISDPHAagDLLCT----------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  628 DIAEILLAAKCDLHAVNIHGD-SPLH----IAARENRYDCVVLFLSRDSDVTLKNKEGETP--LQCASLNSQVW 694
Cdd:PLN03192   669 DMVRLLIMNGADVDKANTDDDfSPTElrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrLQGTSSDNQCR 742
Ank_4 pfam13637
Ankyrin repeats (many copies);
581-634 2.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370515101  581 GWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILL 634
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
566-613 5.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 5.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1370515101  566 LLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNE 613
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
533-588 5.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 5.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  533 LIKAG-ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWA 588
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
633-687 2.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  633 LLAAK-CDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCA 687
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
450-576 4.38e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 4.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  450 LYFSARQGELQKVLLMLVDGIdpNFKMEHQNKRSPLHAAAEAGHVDICHMLVQ-AGANIDTCSEDQrtpLMEAAENNHLE 528
Cdd:PLN03192   562 LHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILYHfASISDPHAAGDL---LCTAAKRNDLT 636
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370515101  529 AVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 576
Cdd:PLN03192   637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA-DVDK 683
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
845-971 1.59e-06

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 48.14  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVCEyvgelisdseadvreEDSYLFDLDN---KDGEVYCIDARFYGNVSRFiNHHCEPNLVpvrvf 921
Cdd:cd20071     10 GRGLVATRDIEPGELILV---------------EKPLVSVPSNsfsLTDGLNEIGVGLFPLASLL-NHSCDPNAV----- 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  922 maHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWD--------IKGKLFSCRCgsPKC 971
Cdd:cd20071     69 --VVFDGNGTLRVRALRDIKAGEELTISYIDPLLPrterrrelLEKYGFTCSC--PRC 122
Ank_5 pfam13857
Ankyrin repeats (many copies);
600-654 1.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  600 LLSKGS-DINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIA 654
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
494-575 3.16e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  494 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV 562
Cdd:PTZ00322    84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                           90
                   ....*....|...
gi 1370515101  563 VQYLLSNGQMDVN 575
Cdd:PTZ00322   164 VQLLSRHSQCHFE 176
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
845-952 4.14e-06

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.


Pssm-ID: 380937  Cd Length: 138  Bit Score: 47.40  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVCEYVGEL--ISDSEADvrEEDSYLFDLDNKDGE---VYCIDARfyGNVSRFI----NHHCE--- 912
Cdd:cd10539     15 GFTVEADGFIKDLTIIAEYTGDVdyIRNREFD--DNDSIMTLLLAGDPSkslVICPDKR--GNIARFIsginNHTKDgkk 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370515101  913 -PNLVPVRVFMAHQdlrfPRIAFFSTRLIEAGEQLGFDYGE 952
Cdd:cd10539     91 kQNCKCVRYSINGE----ARVLLVATRDIAKGERLYYDYNG 127
PHA02875 PHA02875
ankyrin repeat protein; Provisional
558-755 5.93e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 5.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  558 GHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAK 637
Cdd:PHA02875    13 GELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  638 CDLHAVNIH-GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwsalQMSKALQDSApdrpspver 716
Cdd:PHA02875    92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI----KGIELLIDHK--------- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370515101  717 iVSRDIARGYERIP-IPCVNAVDSEPCP------SNYKYVSQN-CVT 755
Cdd:PHA02875   159 -ACLDIEDCCGCTPlIIAMAKGDIAICKmlldsgANIDYFGKNgCVA 204
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
581-612 6.51e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 6.51e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1370515101  581 GWTPMIWA-TEYKHVDLVKLLLSKGSDINIRDN 612
Cdd:pfam00023    2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
848-951 6.97e-06

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 46.42  E-value: 6.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  848 VRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFD--------LDNKDGEVYCIDARFYGNVSRFINHHCEPNlVPVR 919
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQF---EANGYFFKrpypfvlfYSKFHGLEMCVDARTFGNEARFIRRSCTPN-AEVR 96
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370515101  920 VFMAHQDLrfpRIAFFSTRLIEAGEQL----GFDYG 951
Cdd:cd19182     97 HVIEDGTI---HLYIYSIRSIPKGTEItiafDFDYG 129
PHA03100 PHA03100
ankyrin repeat protein; Provisional
461-545 8.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 8.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  461 KVLLMLVDGIDPNFKmehqNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGA 538
Cdd:PHA03100   174 RVNYLLSYGVPINIK----DVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                   ....*..
gi 1370515101  539 LVDPKDA 545
Cdd:PHA03100   250 SIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
513-602 8.65e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 8.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  513 DQRTPLMEAAENNHLEA------VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMI 586
Cdd:PTZ00322    75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153
                           90
                   ....*....|....*.
gi 1370515101  587 WATEYKHVDLVKLLLS 602
Cdd:PTZ00322   154 LAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
515-610 1.00e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.69  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  515 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 581
Cdd:TIGR00870   53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128
                           90       100
                   ....*....|....*....|....*....
gi 1370515101  582 WTPMIWATEYKHVDLVKLLLSKGSDINIR 610
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
546-576 1.09e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.09e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1370515101   546 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 576
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
647-699 1.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370515101  647 GDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVwSALQM 699
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV-EVLKL 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
546-579 1.37e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1370515101  546 EGSTCLHLAAKK-GHYEVVQYLLSNGQmDVNCQDD 579
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
480-508 1.48e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.48e-05
                            10        20
                    ....*....|....*....|....*....
gi 1370515101   480 NKRSPLHAAAEAGHVDICHMLVQAGANID 508
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
828-914 2.04e-05

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 45.77  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  828 VQNGLRARLQLYRTRdmgwgVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDSYLFDL--DNKDGEVYCIDARFYGN 902
Cdd:cd19181      6 LQLGRVTRVQKHRKI-----LRAARDLALDTLIIEYRGKVMLRQQFEVNGhffKRPYPFVLfySKFNGVEMCVDARTFGN 80
                           90
                   ....*....|..
gi 1370515101  903 VSRFINHHCEPN 914
Cdd:cd19181     81 DARFIRRSCTPN 92
Ank_5 pfam13857
Ankyrin repeats (many copies);
500-554 2.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  500 LVQAG-ANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 554
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
597-668 3.04e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370515101  597 VKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLS 668
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
581-609 4.11e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 4.11e-05
                            10        20
                    ....*....|....*....|....*....
gi 1370515101   581 GWTPMIWATEYKHVDLVKLLLSKGSDINI 609
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
522-684 4.15e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.60  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  522 AENNHLEAVKYLIKAGALVDPKDAEGSTCLHlaakkghyevvQYLLSNgqmdvncqddggwtpmiwateYKHVDLVKLLL 601
Cdd:PHA02716   292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  602 SKGSDINIRDNEENICLHwaafsgcvdiaeILLAAKCDLHAVNIHGDSPLhiaarenRYDCVVLFLSRDSDVTLKNKEGE 681
Cdd:PHA02716   340 EYGNDLNEPDNIGNTVLH------------TYLSMLSVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGY 400

                   ...
gi 1370515101  682 TPL 684
Cdd:PHA02716   401 TPL 403
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
630-690 4.49e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370515101  630 AEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLN 690
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
454-535 6.83e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 6.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  454 ARQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYL 533
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                   ..
gi 1370515101  534 IK 535
Cdd:PTZ00322   168 SR 169
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
845-956 6.83e-05

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 43.01  E-value: 6.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  845 GWGVRSLQDIPPGTFVcEYVGELISDSEADVREEDSYLFDLdnkdgeVYCIDARFY----GNVSRFiNHHCEPNLVPVRV 920
Cdd:cd10540     11 GRGVFATRPIKKGEVI-EEAPVIVLPKEEYQHLCKTVLDHY------VFSWGDGCLalalGYGSMF-NHSYTPNAEYEID 82
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1370515101  921 FMAHqdlrfpRIAFFSTRLIEAGEQLGFDYGERFWD 956
Cdd:cd10540     83 FENQ------TIVFYALRDIEAGEELTINYGDDLWD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
480-508 9.12e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 9.12e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370515101  480 NKRSPLHAAAE-AGHVDICHMLVQAGANID 508
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
554-676 1.25e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  554 AAKKGHYEVVQYLLSNGQMD-VNCQDDGGWTPMIW-ATEYKHVDLVKLLLSKGSDINIRDNeeniCLHWAA---FSGCVD 628
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLnINCPDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDT----LLHAISleyVDAVEA 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370515101  629 IAEILLAAKCD----LHAVNI------HGDSPLHIAARENRYDCVVLFLSRDSDVTLK 676
Cdd:TIGR00870  100 ILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02989 PHA02989
ankyrin repeat protein; Provisional
464-637 1.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.50  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  464 LMLVDGIDPNfkmEHQNKR--SPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLEAVKYLI 534
Cdd:PHA02989   129 FLLSKGINVN---DVKNSRgyNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLI 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  535 KAGALVDPKDAEGSTCL------HLAAKKGHYEVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDIN 608
Cdd:PHA02989   206 KKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
                          170       180
                   ....*....|....*....|....*....
gi 1370515101  609 IRDNEENICLHWAAFSGCVDIAEILLAAK 637
Cdd:PHA02989   284 NVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
513-541 1.67e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.67e-04
                            10        20
                    ....*....|....*....|....*....
gi 1370515101   513 DQRTPLMEAAENNHLEAVKYLIKAGALVD 541
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
461-687 3.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 3.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  461 KVLLMLVD-GIDPNFK--MEhqnkrSPLHAAAEAGHVD------ICHMLVQAGANIDTCSEDQRTPLMEAAEN---NHLE 528
Cdd:PHA02989    51 KIVKLLIDnGADVNYKgyIE-----TPLCAVLRNREITsnkikkIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  529 AVKYLIKAGALV-DPKDAEGSTCLH--LAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPM-IW---ATEYKHVDLVKLLL 601
Cdd:PHA02989   126 MLRFLLSKGINVnDVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNLFEKTSLYGLTPMnIYlrnDIDVISIKVIKYLI 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  602 SKGSDInirdnEENICLHWAAFSGCVDIAEILLAaKC-----------DLHAVNIHGDSPLHIAARENRYDCVVLFLSRD 670
Cdd:PHA02989   206 KKGVNI-----ETNNNGSESVLESFLDNNKILSK-KEfkvlnfilkyiKINKKDKKGFNPLLISAKVDNYEAFNYLLKLG 279
                          250
                   ....*....|....*..
gi 1370515101  671 SDVTLKNKEGETPLQCA 687
Cdd:PHA02989   280 DDIYNVSKDGDTVLTYA 296
PHA02859 PHA02859
ankyrin repeat protein; Provisional
507-653 3.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  507 IDTCSEDQRTPLMEAAENNH--LEAVKYLIKAGALVDPK-DAEGSTCLH--LAAKKG-HYEVVQYLLSNGQmDVNCQDDG 580
Cdd:PHA02859    44 VNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtRDNNLSALHhyLSFNKNvEPEILKILIDSGS-SITEEDED 122
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  581 GWTPM-IWATEYK-HVDLVKLLLSKGSDINIRDNEENICLH-WAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHI 653
Cdd:PHA02859   123 GKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
513-544 4.75e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.75e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1370515101  513 DQRTPLMEAAE-NNHLEAVKYLIKAGALVDPKD 544
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
646-675 4.87e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.87e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1370515101   646 HGDSPLHIAARENRYDCVVLFLSRDSDVTL 675
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
552-634 5.25e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  552 HLAAKkGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAE 631
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                   ...
gi 1370515101  632 ILL 634
Cdd:PTZ00322   166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
646-678 6.08e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 6.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1370515101  646 HGDSPLHIAA-RENRYDCVVLFLSRDSDVTLKNK 678
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
583-656 8.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 8.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  583 TPMIWATEYKHVDLVKLLLSKGSDINIRDNEENIC-LHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAAR 656
Cdd:PHA02884    72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
581-609 9.52e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 9.52e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370515101  581 GWTPMIWATEYKHVDLVKLLLSKGSDINI 609
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
546-576 1.11e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.11e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1370515101  546 EGSTCLHLAAKKGHYEVVQYLLSNGqMDVNC 576
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
480-509 1.17e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370515101  480 NKRSPLHAAAEAGHVDICHMLVQAGANIDT 509
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
513-538 1.18e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.18e-03
                           10        20
                   ....*....|....*....|....*.
gi 1370515101  513 DQRTPLMEAAENNHLEAVKYLIKAGA 538
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
842-954 1.77e-03

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 39.52  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  842 RDMGWGVRSLQDIPPGTFVCEYVGELISDSEAdvrEEDSYLFDLDNKDGEVYCIDAR--FYGNVSRFIN---HHCEPNLV 916
Cdd:cd19193     16 PGAGLGVWAEAPIPKGMVFGPYEGEIVEDEEA---ADSGYSWQIYKGGKLSHYIDAKdeSKSNWMRYVNcarNEEEQNLV 92
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1370515101  917 pvrvfmAHQDLRfpRIAFFSTRLIEAGEQLGFDYGERF 954
Cdd:cd19193     93 ------AFQYRG--KIYYRTCKDIAPGTELLVWYGDEY 122
PHA02946 PHA02946
ankyin-like protein; Provisional
465-651 4.59e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  465 MLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPL--MEAAENNHLEAVKYLIKAGALVDP 542
Cdd:PHA02946    58 LLHRGYSPNETDDDGN--YPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINN 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  543 K-DAEGSTCLhLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPM--IWATEYKHVDLVKLLLSKGSDINIRDNEENICLH 619
Cdd:PHA02946   136 SvDEEGCGPL-LACTDPSERVFKKIMSIG-FEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370515101  620 WAAFSGC--VDIAEILLAAKcDLHAVNIHGDSPL 651
Cdd:PHA02946   214 IVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
500-619 5.10e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  500 LVQAGANIDTCSEDQRTPLMEAAENNhlEAVKYLIKAGALVDPkdAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDD 579
Cdd:cd21882     30 LHKAALNLNDGVNEAIMLLLEAAPDS--GNPKELVNAPCTDEF--YQGQTALHIAIENRNLNLVRLLVENGA-DVSARAT 104
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370515101  580 G-------------GWTPMIWATEYKHVDLVKLLLSKGSDI---NIRDNEENICLH 619
Cdd:cd21882    105 GrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
PHA02859 PHA02859
ankyrin repeat protein; Provisional
483-608 7.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  483 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLEAVKYLIKAGALVDPKDAEGSTCLH--LA 554
Cdd:PHA02859    53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370515101  555 AKKGHYEVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKHVDlvkLLLSKGSDIN 608
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKKIFD---FLTSLGIDIN 186
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
844-976 7.57e-03

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 38.03  E-value: 7.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370515101  844 MGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDL----DNKDGEvycidARFYGNVSRFINHHCEPN--LVP 917
Cdd:cd10524     18 YGAKIIATKPIKKGEKIHELCGCIAELSEEEEALLRPGGNDFsvmySSRKKC-----SQLWLGPAAFINHDCRPNckFVP 92
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370515101  918 VRVfmahqdlrfPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKlfSCRCGSpkCRHSSA 976
Cdd:cd10524     93 TGK---------STACVKVLRDIEPGEEITVYYGDNYFGENNE--ECECET--CERRGR 138
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
626-693 8.74e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 8.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370515101  626 CVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLsrDSDVTLKNK-------EGETPLQCASLNSQV 693
Cdd:cd22192     30 VQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIAVVNQNL 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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